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P10795 (RBS1A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase small chain 1A, chloroplastic

Short name=RuBisCO small subunit 1A
EC=4.1.1.39
Gene names
Name:RBCS-1A
Synonyms:ATS1A
Ordered Locus Names:At1g67090
ORF Names:F1O19.14, F5A8.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity.

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

Subunit structure

8 large chains + 8 small chains.

Subcellular location

Plastidchloroplast membrane; Peripheral membrane protein. Plastidchloroplast stroma Ref.6.

Miscellaneous

There are four genes coding for RBS in Arabidopsis thaliana.

Sequence similarities

Belongs to the RuBisCO small chain family.

Sequence caution

The sequence AAK49590.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA31948.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCalvin cycle
Carbon dioxide fixation
Photorespiration
Photosynthesis
   Cellular componentChloroplast
Membrane
Plastid
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Molecular functionLyase
Monooxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchloroplast ribulose bisphosphate carboxylase complex biogenesis

Inferred from mutant phenotype PubMed 22223809. Source: TAIR

photorespiration

Inferred from electronic annotation. Source: UniProtKB-KW

photosynthesis

Inferred from mutant phenotype PubMed 22223809. Source: TAIR

reductive pentose-phosphate cycle

Inferred from electronic annotation. Source: UniProtKB-KW

response to blue light

Inferred from expression pattern PubMed 18820083. Source: TAIR

response to cold

Inferred from expression pattern PubMed 14535880. Source: TAIR

response to far red light

Inferred from expression pattern PubMed 18820083. Source: TAIR

response to red light

Inferred from expression pattern PubMed 18820083. Source: TAIR

   Cellular_componentapoplast

Inferred from direct assay PubMed 18538804. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR

chloroplast envelope

Inferred from direct assay Ref.6PubMed 12938931PubMed 20061580. Source: TAIR

chloroplast membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

chloroplast stroma

Inferred from direct assay PubMed 16207701PubMed 18633119PubMed 20061580. Source: TAIR

chloroplast thylakoid membrane

Inferred from direct assay PubMed 15322131. Source: TAIR

cytosolic ribosome

Inferred from direct assay PubMed 15821981. Source: TAIR

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

thylakoid

Inferred from direct assay PubMed 11826309PubMed 16648217. Source: TAIR

thylakoid lumen

Inferred from direct assay PubMed 11719511. Source: TAIR

   Molecular_functioncopper ion binding

Inferred from direct assay PubMed 16526091. Source: TAIR

monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ribulose-bisphosphate carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P10795-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5555Chloroplast
Chain56 – 180125Ribulose bisphosphate carboxylase small chain 1A, chloroplastic
PRO_0000031463

Amino acid modifications

Modified residue1131Phosphoserine Ref.7

Experimental info

Sequence conflict1151G → R in AAG40356. Ref.4
Sequence conflict1711I → V in CAA31948. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 10, 2003. Version 2.
Checksum: 5DE768676D61F8F7

FASTA18020,216
        10         20         30         40         50         60 
MASSMLSSAT MVASPAQATM VAPFNGLKSS AAFPATRKAN NDITSITSNG GRVNCMQVWP 

        70         80         90        100        110        120 
PIGKKKFETL SYLPDLTDSE LAKEVDYLIR NKWIPCVEFE LEHGFVYREH GNSPGYYDGR 

       130        140        150        160        170        180 
YWTMWKLPLF GCTDSAQVLK EVEECKKEYP NAFIRIIGFD NTRQVQCISF IAYKPPSFTG 

« Hide

References

« Hide 'large scale' references
[1]"Four genes in two diverged subfamilies encode the ribulose-1,5-bisphosphate carboxylase small subunit polypeptides of Arabidopsis thaliana."
Krebbers E., Seurinck J., Herdies L., Cashmore A.R., Timko M.P.
Plant Mol. Biol. 11:745-759(1988) [AGRICOLA] [Europe PMC]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Columbia K85.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Arabidopsis thaliana small subunit leader and transit peptide enhance the expression of Bacillus thuringiensis proteins in transgenic plants."
Wong E.Y., Hironaka C.M., Fishhoff D.A.
Plant Mol. Biol. 20:81-93(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-79.
[6]"Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: cv. Wassilewskija.
[7]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13611 Genomic DNA. Translation: CAA31948.1. Sequence problems.
AC004146 Genomic DNA. Translation: AAD10655.1.
AC007152 Genomic DNA. No translation available.
CP002684 Genomic DNA. Translation: AEE34594.1.
AF325011 mRNA. Translation: AAG40363.1.
AF325004 mRNA. Translation: AAG40356.1.
AF372874 mRNA. Translation: AAK49590.1. Different initiation.
AF410291 mRNA. Translation: AAK95277.1.
AY054188 mRNA. Translation: AAL06849.1.
AY054581 mRNA. Translation: AAK96772.1.
AY058831 mRNA. Translation: AAL24219.1.
AY059940 mRNA. Translation: AAL24422.1.
AY062612 mRNA. Translation: AAL32690.1.
AY062711 mRNA. Translation: AAL32789.1.
AY065101 mRNA. Translation: AAL38277.1.
AY093380 mRNA. Translation: AAM13379.1.
AY093388 mRNA. Translation: AAM13387.1.
AY097366 mRNA. Translation: AAM19882.1.
BT000362 mRNA. Translation: AAN15681.1.
BT002076 mRNA. Translation: AAN72087.1.
X68342 Other DNA. Translation: CAA48415.1. Different termination.
PIRG96694.
RKMUA1. S03720.
RefSeqNP_176880.1. NM_105379.3. [P10795-1]
UniGeneAt.12721.
At.30194.
At.37531.
At.46639.
At.49098.
At.67454.
At.68122.
At.70032.
At.70053.

3D structure databases

ProteinModelPortalP10795.
SMRP10795. Positions 56-178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid28250. 5 interactions.
IntActP10795. 6 interactions.
MINTMINT-2584041.

2D gel databases

World-2DPAGE0003:P10795.

Proteomic databases

PaxDbP10795.
PRIDEP10795.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G67090.1; AT1G67090.1; AT1G67090. [P10795-1]
GeneID843029.
KEGGath:AT1G67090.

Organism-specific databases

TAIRAT1G67090.

Phylogenomic databases

eggNOGCOG4451.
HOGENOMHOG000141332.
InParanoidP10795.
KOK01602.
OMAAFPATRK.
PhylomeDBP10795.

Enzyme and pathway databases

BioCycARA:GQT-1261-MONOMER.
MetaCyc:AT1G67090-MONOMER.

Gene expression databases

GenevestigatorP10795.

Family and domain databases

Gene3D3.30.190.10. 1 hit.
InterProIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSPR00152. RUBISCOSMALL.
SMARTSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMSSF55239. SSF55239. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRBS1A_ARATH
AccessionPrimary (citable) accession number: P10795
Secondary accession number(s): Q94JW2, Q9FPI6, Q9SAV4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 10, 2003
Last modified: July 9, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names